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KIB1_ARATH
ID   KIB1_ARATH              Reviewed;         382 AA.
AC   Q9SU05;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=F-box/kelch-repeat protein KIB1 {ECO:0000303|PubMed:28575660};
DE   AltName: Full=Protein KINK SUPPRESSED IN BZR1-1D 1 {ECO:0000303|PubMed:28575660};
GN   Name=KIB1 {ECO:0000303|PubMed:28575660};
GN   OrderedLocusNames=At4g12810 {ECO:0000312|Araport:AT4G12810};
GN   ORFNames=T20K18.160 {ECO:0000312|EMBL:CAB40998.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SKP1A/ASK1; ASK1/SK11;
RP   ASK3/SK12; ASK5/SK13; ASK7/BIN2/SK21; ASK9/SK22 AND ASK6/SK23, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia, and cv. Wassilewskija;
RX   PubMed=28575660; DOI=10.1016/j.molcel.2017.05.012;
RA   Zhu J.-Y., Li Y., Cao D.-M., Yang H., Oh E., Bi Y., Zhu S., Wang Z.-Y.;
RT   "The F-box protein KIB1 mediates brassinosteroid-induced inactivation and
RT   degradation of GSK3-like kinases in Arabidopsis.";
RL   Mol. Cell 66:648-657(2017).
CC   -!- FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase
CC       complexes, which may mediate the ubiquitination and subsequent
CC       proteasomal degradation of target proteins. Required for
CC       brassinosteroid (BR) signal transduction. Mediates ASK7/BIN2/SK21
CC       inactivation both by competing with substrate binding (e.g. BZR1) and
CC       by promoting its ubiquitination and subsequent proteasomal degradation.
CC       {ECO:0000269|PubMed:28575660}.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       Binds directly to several GSK3 family proteins such as SKP1A/ASK1,
CC       ASK1/SK11, ASK3/SK12, ASK5/SK13, ASK7/BIN2/SK21, ASK9/SK22 and
CC       ASK6/SK23. Interacts with ASK7/BIN2/SK21 in a brassinosteroid (BR)-
CC       dependent manner. {ECO:0000269|PubMed:28575660}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28575660}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:28575660}. Note=Mostly localized in the
CC       nucleolus, and, to a lower extent, in the cytoplasm.
CC       {ECO:0000269|PubMed:28575660}.
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, stems, flower buds
CC       and flowers. {ECO:0000269|PubMed:28575660}.
CC   -!- DISRUPTION PHENOTYPE: Abolished brassinosteroid (BR)-induced
CC       ASK7/BIN2/SK21 degradation, and severe BR-insensitivity. Suppression of
CC       the constitutive BR-response phenotype in the dominant mutant bzr1-1D,
CC       and accumulation of phosphorylated BZR1. {ECO:0000269|PubMed:28575660}.
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DR   EMBL; AL049640; CAB40998.1; -; Genomic_DNA.
DR   EMBL; AL161534; CAB78323.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83187.1; -; Genomic_DNA.
DR   PIR; T06639; T06639.
DR   RefSeq; NP_193017.1; NM_117350.1.
DR   AlphaFoldDB; Q9SU05; -.
DR   SMR; Q9SU05; -.
DR   STRING; 3702.AT4G12810.1; -.
DR   iPTMnet; Q9SU05; -.
DR   PaxDb; Q9SU05; -.
DR   PRIDE; Q9SU05; -.
DR   EnsemblPlants; AT4G12810.1; AT4G12810.1; AT4G12810.
DR   GeneID; 826893; -.
DR   Gramene; AT4G12810.1; AT4G12810.1; AT4G12810.
DR   KEGG; ath:AT4G12810; -.
DR   Araport; AT4G12810; -.
DR   TAIR; locus:2135823; AT4G12810.
DR   eggNOG; ENOG502S0MJ; Eukaryota.
DR   HOGENOM; CLU_019286_7_1_1; -.
DR   InParanoid; Q9SU05; -.
DR   OMA; HFRSANV; -.
DR   OrthoDB; 820958at2759; -.
DR   PhylomeDB; Q9SU05; -.
DR   PRO; PR:Q9SU05; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SU05; baseline.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IPI:TAIR.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:TAIR.
DR   GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IGI:TAIR.
DR   GO; GO:1900459; P:positive regulation of brassinosteroid mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   InterPro; IPR005174; DUF295.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR   Pfam; PF03478; DUF295; 1.
DR   Pfam; PF00646; F-box; 1.
DR   SUPFAM; SSF50965; SSF50965; 1.
PE   1: Evidence at protein level;
KW   Brassinosteroid signaling pathway; Cytoplasm; Kelch repeat; Nucleus;
KW   Reference proteome; Repeat; Ubl conjugation pathway.
FT   CHAIN           1..382
FT                   /note="F-box/kelch-repeat protein KIB1"
FT                   /id="PRO_0000283242"
FT   DOMAIN          22..69
FT                   /note="F-box"
FT                   /evidence="ECO:0000255"
FT   REPEAT          73..117
FT                   /note="Kelch 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          159..209
FT                   /note="Kelch 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          259..306
FT                   /note="Kelch 3"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   382 AA;  44034 MW;  6CB0D36BC3CAC404 CRC64;
     MTHKKQKKEM SDSEKKTFNE DSKHSILAVD LVRLILERLS FVDFHRARCV SSIWYIASKT
     VIGVTNPTTP WLILFPKGDV EIKKDSCKLY DPHENKTYIV RDLGFDLVTS RCLASSGSWF
     LMLDHRTEFH LLNLFTRVRI PLPSLESTRG SDIKIGNAVL WVDEQRKDYL VVWNISSLFG
     YHKKGDDRWK VFKPLENERC IIAMVFKENK LYVLSVDGNV DVFYFSGNDS PVRCATLPSS
     PLRKGHKVVV TLSGEVLIIV AKVEPYPRTR LCFFAVYKMD PKSSRWETIK SLAGEALILD
     LGITVEAKVM KNCIYFSNDQ FHRYNENSLW NVSNKSGVFV YHFRSANVVQ LVELLTASSR
     TSKILFKDAR CFFPTFTSKW LL
 
 
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